Acetylation Mass Spectrometry
Acetylation Mass Spectrometry is a post-translational modification (PTM) analysis method based on mass spectrometry technology. It is specifically used for detecting and identifying acetylation modification sites on proteins and performing qualitative and quantitative analysis. Acetylation is an important form of protein post-translational modification, widely present in both eukaryotic and prokaryotic proteins, and plays a role in regulating gene expression, metabolic processes, cell cycle, and signal transduction, among other crucial biological processes. The advent of acetylation mass spectrometry allows researchers to deeply analyze the dynamic changes and functional significance of protein acetylation within cells, providing a powerful tool for uncovering disease mechanisms and discovering drug targets. In cancer research, acetylation mass spectrometry is used to reveal abnormal acetylation states of cancer-related proteins, aiding in the search for new therapeutic targets. In neurodegenerative diseases such as Parkinson's and Alzheimer's, acetylation modification plays an important role in regulating neuron survival and apoptosis. In metabolic diseases like diabetes and obesity, acetylation modification plays a key role in the regulation of insulin signaling pathways and metabolic enzyme activity. Using acetylation mass spectrometry, inhibitors of acetylation enzymes (HATs/HDACs) can be screened, leading to the development of novel drugs.
1. Principle of Acetylation Mass Spectrometry
Acetylation mass spectrometry utilizes high-resolution mass spectrometers combined with highly specific acetylation site enrichment techniques to achieve precise detection and analysis of protein acetylation modifications. The main principles include the following steps:
1. Protein Extraction and Digestion
Total proteins are extracted from biological samples and degraded into peptides using enzymes such as trypsin.
2. Enrichment of Acetylated Peptides
Since acetylated peptides comprise a small proportion of total peptides, direct detection is challenging. Therefore, acetylated peptides need to be enriched using specific antibodies (such as anti-acetyllysine antibodies) or affinity chromatography methods.
3. Liquid Chromatography-Mass Spectrometry (LC-MS/MS)
Liquid chromatography is used to separate enriched acetylated peptides, followed by tandem mass spectrometry (MS/MS) to fragment the peptides and analyze the acetylation modification sites and their sequence information.
4. Data Analysis
Specialized bioinformatics software (such as MaxQuant, Proteome Discoverer, etc.) is used to analyze mass spectrometry data, determining specific acetylation modification sites and performing qualitative and quantitative analysis.
2. Advantages of Acetylation Mass Spectrometry
1. High Specificity and Sensitivity
Acetylation mass spectrometry can accurately detect low-abundance acetylated peptides in complex biological samples, with sensitivity and specificity significantly higher than traditional detection methods.
2. Comprehensive Modification Site Identification
Using high-resolution mass spectrometry technology, thousands of acetylation modification sites can be detected in a single experiment, revealing the global acetylation status of proteins.
3. Dynamic Quantitative Analysis
By combining labeling techniques (such as SILAC, TMT, iTRAQ), acetylation mass spectrometry allows for dynamic comparison and quantitative analysis of acetylation levels in different samples or at different time points.
4. Functional Analysis
Combining bioinformatics analysis, acetylation modifications can be deeply analyzed for functional changes in specific cell pathways or disease models.
With extensive experience in proteomics analysis and advanced mass spectrometry platforms, Biotyper Biosciences provides high-quality acetylation quantitative proteomics research services to researchers and pharmaceutical companies. We look forward to working with you to uncover the mysteries of acetylation modifications!
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